ID F3GCE7_PSESJ Unreviewed; 308 AA.
AC F3GCE7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|RuleBase:RU000579};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|RuleBase:RU000579};
GN ORFNames=PSYPI_21205 {ECO:0000313|EMBL:EGH44747.1};
OS Pseudomonas syringae pv. pisi str. 1704B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH44747.1, ECO:0000313|Proteomes:UP000004986};
RN [1] {ECO:0000313|EMBL:EGH44747.1, ECO:0000313|Proteomes:UP000004986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1704B {ECO:0000313|EMBL:EGH44747.1,
RC ECO:0000313|Proteomes:UP000004986};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADH; Xref=Rhea:RHEA:15757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001406};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC Evidence={ECO:0000256|RuleBase:RU000579};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC {ECO:0000256|RuleBase:RU000579}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5. {ECO:0000256|RuleBase:RU000579}.
CC -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006753, ECO:0000256|RuleBase:RU004171}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGH44747.1}.
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DR EMBL; AEAI01001068; EGH44747.1; -; Genomic_DNA.
DR AlphaFoldDB; F3GCE7; -.
DR PATRIC; fig|629263.4.peg.3443; -.
DR HOGENOM; CLU_009116_1_2_6; -.
DR BioCyc; PSYR629263:G11X0-4144-MONOMER; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000004986; Unassembled WGS sequence.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001342; HDH_cat.
DR InterPro; IPR019811; HDH_CS.
DR InterPro; IPR022697; HDH_short.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43331; HOMOSERINE DEHYDROGENASE; 1.
DR PANTHER; PTHR43331:SF1; HOMOSERINE DEHYDROGENASE; 1.
DR Pfam; PF00742; Homoserine_dh; 1.
DR PIRSF; PIRSF036497; HDH_short; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU000579};
KW Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU000579};
KW Isoleucine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW Methionine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW NADP {ECO:0000256|PIRSR:PIRSR036497-2, ECO:0000256|RuleBase:RU000579};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000579};
KW Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT DOMAIN 119..297
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
FT ACT_SITE 186
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-1"
FT BINDING 87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
SQ SEQUENCE 308 AA; 31920 MW; FB8E87C86735CABD CRC64;
MSDIFLGSVI AKDGLDPNEL AAVPAAKGAF ATLANGNAEP DNETVIRFSG ADIVAEATFT
NPVDGEPATT FCRWALDQGI SVVTTNKGPV ALRCAELKKL AQKSGAAFEF EGAVMSGTPV
IRMAQEVLAG SEITGFKGIL NGTSNFILSS MQEGLDFGRA LIKAQEMGYA EADPTADVEG
HDVRLKVVIL ANELLGAKLT PNDVSCEGIS KITTQDIQSA ARQDSRWKLI GSATRSPSGV
VSATVSPQLL PNSDALAGVS GATNAVSFQT NLLGPVTISG AGAGRVETAY ALLSDIISIH
KNKTKRAI
//
